title: Cyclic α,β-tetrapeptoids: sequence-dependent cyclization and conformational preference.
abstract: The presence of at least one N-Cα branched side chain is crucial for successful cyclization of α,β-tetrapeptoids. The ctct amide sequence revealed in the crystal structure of the 14-membered cyclotetrapeptoid 8 is also the most populated conformation in solution and is reminiscent of the predominant amide arrangement of the 12-membered cyclic tetrapeptides (CTPs).
authors.affiliation: Clermont Université, Université Blaise Pascal, Institut de Chimie de Clermont-Ferrand, BP10448, F-63000 Clermont-Ferrand, France.
authors.forename: Cécile
authors.initials: C
authors.lastname: Caumes
authors.forename: Carlos
authors.initials: C
authors.lastname: Fernandes
authors.forename: Olivier
authors.initials: O
authors.lastname: Roy
authors.forename: Thomas
authors.initials: T
authors.lastname: Hjelmgaard
authors.forename: Emmanuel
authors.initials: E
authors.lastname: Wenger
authors.forename: Claude
authors.initials: C
authors.lastname: Didierjean
authors.forename: Claude
authors.initials: C
authors.lastname: Taillefumier
authors.forename: Sophie
authors.initials: S
authors.lastname: Faure
mesh_terms: D000595:Amino Acid Sequence; D002942:Circular Dichroism; D018360:Crystallography, X-Ray; D003500:Cyclization; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D008968:Molecular Conformation; D009842:Oligopeptides / Q000737:chemistry*; D034444:Peptoids / Q000737:chemistry*
chemical_list: D009842:Oligopeptides; D034444:Peptoids